|
Name |
Accession |
Description |
Interval |
E-value |
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
36-470 |
0e+00 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 649.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 36 EVLAFEGYRITGSDIAHSAMTDRLIKAGAEVFIGHHENNVKDANVVVVSSAIDETNPEIIAAKAARIPVVRRAEMLAELM 115
Cdd:COG0773 22 EILLALGYKVSGSDLAESPMTERLEALGIPVFIGHDAENIDDADLVVVSSAIPRDNPELVAARERGIPVLSRAEMLAELM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 116 RFRHGIAIAGTHGKTTTTSLIASIYGQAGLDPTFIIGGLLNSAGSNAKVGKSDFLIAEADESDASFLHLQPMVSVITNIE 195
Cdd:COG0773 102 RGKRSIAVAGTHGKTTTTSMLAHILEEAGLDPTFLIGGILNNFGTNARLGDGDYFVAEADESDGSFLHYSPDIAVVTNIE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 196 EDHMDTYgGSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYGESKDADYRMSDFSQSANTCTFTVTN 275
Cdd:COG0773 182 ADHLDIY-GDLEAIKEAFHEFARNVPFYGLLVLCADDPGLRELLPRCGRPVITYGFSEDADYRAENIRIDGGGSTFDVLR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 276 KQGECLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGefenERGNVMLVDDYGHHPSEVAA 355
Cdd:COG0773 261 RGEELGEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFELKG----EVGGVTVIDDYAHHPTEIAA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 356 TIAAVREGWPDKRLVMVYQPHRFSRTRDLYEDFVKVLADVDQLLLLDVYSAGEDPIVGADSKSLCRSLRQRGKEPLHVAT 435
Cdd:COG0773 337 TLAAAREKYPDRRLVAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYAAREKPIPGVSSEDLAEAIRKRGKDVVYVPD 416
|
410 420 430
....*....|....*....|....*....|....*
gi 746445361 436 NAELAGVLAANLQNNDLVLTQGAGNIGQLVKTLAA 470
Cdd:COG0773 417 LDELVEALAEIARPGDVVLTMGAGDIGGLGEKLLE 451
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
20-464 |
0e+00 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 575.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 20 TIHFIGIGGAGMGGIAEVLAFEGYRITGSDIAHSAMTDRLIKAGAEVFIGHHENNVKDANVVVVSSAIDETNPEIIAAKA 99
Cdd:TIGR01082 1 KIHFVGIGGIGMSGIAEILLNRGYQVSGSDIAENATTKRLEALGIPIYIGHSAENLDDADVVVVSAAIKDDNPEIVEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 100 ARIPVVRRAEMLAELMRFRHGIAIAGTHGKTTTTSLIASIYGQAGLDPTFIIGGLLNSAGSNAKVGKSDFLIAEADESDA 179
Cdd:TIGR01082 81 RGIPVIRRAEMLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVVVGGLVKEAGTNARLGSGEYLVAEADESDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 180 SFLHLQPMVSVITNIEEDHMDTYGGSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYG-ESKDADYR 258
Cdd:TIGR01082 161 SFLHLQPNVAIVTNIEPDHLDTYGSSFERLKAAFEKFIHNLPFYGLAVICADDPVLRELVPKATEQVITYGgSGEDADYR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 259 MSDFSQSANTCTFTVTNKQGECLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGEFenerG 338
Cdd:TIGR01082 241 AENIQQSGAEGKFSVRGKGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEILGEF----G 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 339 NVMLVDDYGHHPSEVAATIAAVREGWPDKRLVMVYQPHRFSRTRDLYEDFVKVLADVDQLLLLDVYSAGEDPIVGADSKS 418
Cdd:TIGR01082 317 GVLLIDDYAHHPTEIKATLKAARQGYPDKRIVVVFQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAGEEPINGIDGKS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 746445361 419 LCRSLRQRGK-EPLHVATNAELAGVLAANLQNNDLVLTQGAGNIGQL 464
Cdd:TIGR01082 397 LARKITQLGKiEPYFVPDLAELVEFLAAVLQSGDLILTMGAGDIIKL 443
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
15-461 |
2.92e-98 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 313.29 E-value: 2.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 15 MRRIETIHFIGIGGAGMGGIAEVLAFEGYRITGSDIAHSAMTDRLIKAGAEVFIGHHENNVKDANVVVVSSAIDETNPEI 94
Cdd:PRK14573 1 MMKSLFYHFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYSSSISKDNVEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 95 IAAKAARIPVVRRAEMLAELMRFRHGIAIAGTHGKTTTTSLIASIYGQAGLDPTFIIGGlLNSAGSNAKVGKSDFLIAEA 174
Cdd:PRK14573 81 LSAKSRGNRLVHRAELLAELMQEQISILVSGSHGKTTVSSLITAIFQEAKKDPSYAIGG-LNQEGLNGYSGSSEYFVAEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 175 DESDASFLHLQPMVSVITNIEEDHMDTYGGSLEKMKDTYVDFIH-----NLPFYGLAVVCIDSEVAAeliprfgrpvITY 249
Cdd:PRK14573 160 DESDGSLKHYTPEFSVITNIDNEHLSNFEGDRELLLASIQDFARkvqqiNKCFYNGDCPRLKGCLQG----------HSY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 250 GESKDADYRMSDFSQSANTCTFTVTNKQGECLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQH 329
Cdd:PRK14573 230 GFSSSCDLHILSYYQEGWRSYFSAKFLGVVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRLER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 330 ygefENERGNVMLVDDYGHHPSEVAATIAAVREGWPDKRLVMVYQPHRFSRTRDLYEDFVKVLADVDQLLLLDVYSAGED 409
Cdd:PRK14573 310 ----KNSSETFLFLEDYAHHPSEISCTLRAVRDAVGLRRIIAICQPHRFSRLRECLDSFPSAFQDADEVILTDVYSAGEE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 746445361 410 PIVGADSKSLCRSLRQRGKEPLHVATNAELAGVLAANLQNNDLVLTQGAGNI 461
Cdd:PRK14573 386 PEDSISYQKLAEAISQSSIVKCTYVPFHEIQRYLEQSIRVHDVCVSLGAGNI 437
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
38-361 |
9.48e-38 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 143.30 E-value: 9.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 38 LAFEGYRITGSDI--AHSAMTDRLIKAGAEVFIGHH-ENNVKDANVVVVSSAIDETNPEIIAAKAARIPVVrrAEMlaEL 114
Cdd:COG0771 23 LAKLGAEVTVSDDrpAPELAAAELEAPGVEVVLGEHpEELLDGADLVVKSPGIPPDHPLLKAARAAGIPVI--GEI--EL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 115 -MRFRHG--IAIAGTHGKTTTTSLIASIYGQAGLDPtfIIGG-----LLNSAgsnAKVGKSDFLIAEAdeSdaSF-LH-- 183
Cdd:COG0771 99 aYRLSPApiIAITGTNGKTTTTTLIGHILKAAGLRV--AVGGnigtpLLDLL---LEPEPPDVYVLEL--S--SFqLEtt 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 184 --LQPMVSVITNIEEDHMDTYGgSLEKmkdtYVDF----IHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYGESKDADy 257
Cdd:COG0771 170 psLRPDVAVILNITPDHLDRHG-SMEA----YAAAkariFANQTPDDYAVLNADDPLTRALAEEAKARVVPFSLKEPLE- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 258 rmSDFSQSANTCTFtVTNKQGECLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGefenER 337
Cdd:COG0771 244 --GGAGLEDGKLVD-RASGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVA----EI 316
|
330 340
....*....|....*....|....*..
gi 746445361 338 GNVMLVDDyghhpSE---VAATIAAVR 361
Cdd:COG0771 317 NGVRFIND-----SKatnPDATLAALE 338
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
78-373 |
1.30e-34 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 134.82 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 78 ANVVVVssaidETNPEIIAAKAARIPV--VRRAemLAEL-MRFrHG--------IAIAGTHGKTTTTSLIASIYGQAGLd 146
Cdd:COG0769 37 AVAVVT-----EAPGALLAAGVPVIVVpdPRAA--LALLaAAF-YGhpsqklklIGVTGTNGKTTTTYLLAQILRALGK- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 147 PTFIIGGLLNSAGSNAKvgKSDF----------LIAEADESDASF-----------------LHLQpmVSVITNIEEDHM 199
Cdd:COG0769 108 KTGLIGTVGNGIGGELI--PSSLttpealdlqrLLAEMVDAGVTHvvmevsshaldqgrvdgVRFD--VAVFTNLTRDHL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 200 DtYGGSLE-----KMKdtyvdFIHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYGESKDADYRMSDFSQSANTCTFTVT 274
Cdd:COG0769 184 D-YHGTMEayfaaKAR-----LFDQLGPGGAAVINADDPYGRRLAAAAPARVITYGLKADADLRATDIELSADGTRFTLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 275 NKQGEcLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGefenERGNVMLVDDYGHHPSEVA 354
Cdd:COG0769 258 TPGGE-VEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVD----GGQGPTVIVDYAHTPDALE 332
|
330
....*....|....*....
gi 746445361 355 ATIAAVREgWPDKRLVMVY 373
Cdd:COG0769 333 NVLEALRP-HTKGRLIVVF 350
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
36-361 |
1.23e-30 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 123.22 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 36 EVLAFEGYRITGSDIAHSAMTDRLIKA-----GAEVFIGHHENNVKDANVVVVSSAIDETNPEIIAAKAARIPVVRRAEM 110
Cdd:TIGR01087 16 RFLHKKGAEVTVTDLKPNEELEPSMGQlrlneGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLVQAAAKRGIPVVGDIEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 111 LAELMRfRHGIAIAGTHGKTTTTSLIASIYGQAGLdPTFIIGGLLNSAGSNAKVGKSDFLIAEAdesdASF-LH----LQ 185
Cdd:TIGR01087 96 FLRLVP-LPVVAITGTNGKTTTTSLLYHLLKAAGL-KAFLGGNIGTPALEVLDQEGAELYVLEL----SSFqLEttesLR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 186 PMVSVITNIEEDHMDTYGGSLEKMKDTYVDFiHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYGESKDADYRMSDfsqs 265
Cdd:TIGR01087 170 PEIALILNISEDHLDWHGSFEDYVAAKLKIF-ARQTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEKDAERGLCI---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 266 antctftvtNKQGECL---TATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGEFenerGNVML 342
Cdd:TIGR01087 245 ---------RDGGLYLkpnDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQK----NGVHF 311
|
330 340
....*....|....*....|..
gi 746445361 343 VDDyghhpSE---VAATIAAVR 361
Cdd:TIGR01087 312 YND-----SKatnVHATLAALS 328
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
123-303 |
3.00e-30 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 116.63 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 123 IAGTHGKTTTTSLIASIYGQAGLdPTFIIGGLLNSAGSN-------------AKVGKSDFLIAEA-----DESDASFLhL 184
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGG-VIGTIGTYIGKSGNTtnnaiglpltlaeMVEAGAEYAVLEVsshglGEGRLSGL-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 185 QPMVSVITNIEEDHMDtYGGSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELI---PRFGRPVITYGESKDADYRMSD 261
Cdd:pfam08245 79 KPDIAVFTNISPDHLD-FHGTMENYAKAKAELFEGLPEDGIAVINADDPYGAFLIaklKKAGVRVITYGIEGEADLRAAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 746445361 262 FSQSANTCTFTVTNKQGECLTATLNMPGRHNALNATAAIAVA 303
Cdd:pfam08245 158 IELSSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
121-454 |
7.88e-29 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 118.28 E-value: 7.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 121 IAIAGTHGKTTTTSLIASIYGQAGldPTfiigglLNSAGS-NAKVG----------KSDFLIAEADesdASflHL----- 184
Cdd:COG0770 103 IAITGSNGKTTTKEMLAAVLSTKG--KV------LATPGNfNNEIGvpltllrlpeDHEFAVLEMG---MN--HPgeiay 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 185 -----QPMVSVITNIEEDHMDTYGgSLE-----KMKdtyvdFIHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYGESKD 254
Cdd:COG0770 170 lariaRPDIAVITNIGPAHLEGFG-SLEgiaraKGE-----IFEGLPPGGVAVLNADDPLLAALAERAKARVLTFGLSED 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 255 ADYRMSDFSQSANTCTFTVTNKQGEcLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRfqhyGEFE 334
Cdd:COG0770 244 ADVRAEDIELDEDGTRFTLHTPGGE-LEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGR----LEVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 335 NERGNVMLVDD-YGHHPSEVAATIAAVREGWPDKRLVMVyqphrF-------SRTRDLYEDFVKVLAD--VDQLLLldvy 404
Cdd:COG0770 319 EGAGGVTLIDDsYNANPDSMKAALDVLAQLPGGGRRIAV-----LgdmlelgEESEELHREVGELAAElgIDRLFT---- 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 746445361 405 sagedpiVGADSKSLCRSLRQRGKEplHVATNAELAGVLAANLQNNDLVL 454
Cdd:COG0770 390 -------VGELARAIAEAAGGERAE--HFEDKEELLAALKALLRPGDVVL 430
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
59-334 |
2.63e-20 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 93.11 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 59 LIKAGAEVFIGHH-ENNVKDANVVVVSSAIDETNPEIIAAKAARIPVVRRAEMLAELMRfRHGIAIAGTHGKTTTTSLIA 137
Cdd:PRK14106 49 LGELGIELVLGEYpEEFLEGVDLVVVSPGVPLDSPPVVQAHKKGIEVIGEVELAYRFSK-APIVAITGTNGKTTTTTLLG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 138 SIYGQAGlDPTFI---IGGLLNSAGSNAkvGKSDFLIAEAdesdASF-----LHLQPMVSVITNIEEDHMDTYgGSLEKM 209
Cdd:PRK14106 128 EIFKNAG-RKTLVagnIGYPLIDAVEEY--GEDDIIVAEV----SSFqletiKEFKPKVGCILNITPDHLDRH-KTMENY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 210 KDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFGRPVITYgeSKDADYRMSDFSQSANTCTFTVTNKQGECLTATLNMPG 289
Cdd:PRK14106 200 IKAKARIFENQRPSDYTVLNYDDPRTRSLAKKAKARVIFF--SRKSLLEEGVFVKNGKIVISLGGKEEEVIDIDEIFIPG 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 746445361 290 RHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYGEFE 334
Cdd:PRK14106 278 EHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAEIN 322
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
121-362 |
6.06e-19 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 89.04 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 121 IAIAGTHGKTTTTSLIASIYGQAGLdPTFIIGGLLNsaGSNAKVGKSDF----------LIAEADESDASFL------H- 183
Cdd:PRK00139 98 IGVTGTNGKTTTAYLLAQILRLLGE-KTALIGTLGN--GIGGELIPSGLttpdaldlqrLLAELVDAGVTYAamevssHa 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 184 --------LQPMVSVITNIEEDHMDtYGGSLE-----KMKdtyvdFIHNLpfYGLAVVCIDSEVAAELIPRFGRPVITYg 250
Cdd:PRK00139 175 ldqgrvdgLKFDVAVFTNLSRDHLD-YHGTMEdylaaKAR-----LFSEL--GLAAVINADDEVGRRLLALPDAYAVSM- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 251 esKDADYRMSDFSQSANTCTFTVTNkqgeclTATLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHY 330
Cdd:PRK00139 246 --AGADLRATDVEYTDSGQTFTLVT------EVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERV 317
|
250 260 270
....*....|....*....|....*....|..
gi 746445361 331 GefenERGNVMLVDDYGHHPSEVAATIAAVRE 362
Cdd:PRK00139 318 D----AGQGPLVIVDYAHTPDALEKVLEALRP 345
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
39-351 |
1.18e-16 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 81.98 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 39 AFEGYRITGSDIAHSAMtdrlikagaevfighhENNvkdANVVVVSSAIDETNPEIIAAKAARipvvRRAEMLAELMRF- 117
Cdd:TIGR01085 22 AIKGTHVDGHDFIHDAI----------------ANG---AVAVVVERDVDFYVAPVPVIIVPD----LRHALSSLAAAFy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 118 ----RHG--IAIAGTHGKTTTTSLIASIYGQAGLDPTFI------IGG----------------LLNSAGSNAKVGKSDF 169
Cdd:TIGR01085 79 ghpsKKLkvIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIgtigyrLGGndliknpaalttpealTLQSTLAEMVEAGAQY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 170 LIAEAdESDASFLH-LQPM---VSVITNIEEDHMDtYGGSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFGRP 245
Cdd:TIGR01085 159 AVMEV-SSHALAQGrVRGVrfdAAVFTNLSRDHLD-FHGTMENYFAAKASLFTELGLKRFAVINLDDEYGAQFVKRLPKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 246 VITYGESKDADYRMSDFSQSANTC-----TFTVTNKQGEcLTATLNMPGRHNALNATAAIAVAKDQ-NIANHAILEALQK 319
Cdd:TIGR01085 237 ITVSAITQPADGRAQDIKITDSGYsfegqQFTFETPAGE-GHLHTPLIGRFNVYNLLAALATLLHLgGIDLEDIVAALEK 315
|
330 340 350
....*....|....*....|....*....|....
gi 746445361 320 FEGIGRRFQ--HYGEFENergnvMLVdDYGHHPS 351
Cdd:TIGR01085 316 FRGVPGRMElvDGGQKFL-----VIV-DYAHTPD 343
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
39-373 |
2.51e-15 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 78.98 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 39 AFEGYRITGSDIAHSAMTDRLIKAGaEVFI---GHHENN---VKDANVVVVSSAIDETNPE--IIAAKAARIPVVRRAEM 110
Cdd:PRK11929 18 ALAWLRGCVAATADLRLDSREVQPG-DLFVacrGAASDGrafIDQALARGAAAVLVEAEGEdqVAAADALVLPVADLRKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 111 LAELMRFRHG--------IAIAGTHGKTTTTSLIASIYGQAGlDPTFIIGGLLNS------AGSNA-------------- 162
Cdd:PRK11929 97 LGELAARWYGrpseqlslVAVTGTNGKTSCAQLLAQLLTRLG-KPCGSIGTLGARldgrliPGSLTtpdaiilhrilarm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 163 KVGKSDFLIAEADE---SDASFLHLQPMVSVITNIEEDHMDtYGGSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELI 239
Cdd:PRK11929 176 RAAGADAVAMEASShglEQGRLDGLRIAVAGFTNLTRDHLD-YHGTMQDYEEAKAALFSKLPGLGAAVINADDPAAARLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 240 ---PRfGRPVITYGESKDADYRMSDFSQSANTCTFTVTNKQGEcLTATLNMPGRHNALNATAAIAVAKDQNIANHAILEA 316
Cdd:PRK11929 255 aalPR-GLKVGYSPQNAGADVQARDLRATAHGQVFTLATPDGS-YQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARA 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 746445361 317 LQKFEGIGRRFQHYGEFENERGNVMLVdDYGHHPSEVAATIAAVR--EGWPDKRLVMVY 373
Cdd:PRK11929 333 LAAVSPVPGRMERVGPTAGAQGPLVVV-DYAHTPDALAKALTALRpvAQARNGRLVCVF 390
|
|
| Mur_ligase |
pfam01225 |
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ... |
20-119 |
9.27e-15 |
|
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460121 [Multi-domain] Cd Length: 84 Bit Score: 69.19 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 20 TIHFIGIGGAGMGGIAEVLAFEGYRITGSDIAHSamtdrLIKAGAEVFIGHHENNvkdanvvvvssAIDETNPEIIAAKA 99
Cdd:pfam01225 1 EIHFVGIDGRGMSPGALFLALKGYRVDGSDFIES-----LIALGAAAVVGHDAAN-----------NISPDNPELEAAKV 64
|
90 100
....*....|....*....|
gi 746445361 100 ARIPVVRRAEMLAELMRFRH 119
Cdd:pfam01225 65 PGIPVIDRREALAELAAAFY 84
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
121-457 |
6.01e-14 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 74.36 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 121 IAIAGTHGKTTTTSLIASIYGQAGLDptfiiGGLLNSAGS-NAKVGKSDFLIAEADESDASFLHL--------------- 184
Cdd:PRK11929 606 VAITGSNGKTTTKEMIAAILAAWQGE-----DRVLATEGNfNNEIGVPLTLLRLRAQHRAAVFELgmnhpgeiaylaaia 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 185 QPMVSVITNIEEDHMDTYGgSLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFG-RPVITYGESKDADYRMSDFS 263
Cdd:PRK11929 681 APTVALVTNAQREHQEFMH-SVEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLAGaRRVLRFGLQPGADVYAEKIA 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 264 QSANTC------TFTVTNKQGECLTatLNMPGRHNALNATAAIAVAKDQNIANHAILEALQKFEGIGRRFQHYgefENER 337
Cdd:PRK11929 760 KDISVGeaggtrCQVVTPAGSAEVY--LPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRR---RLSC 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 338 GNVMLVDDYGHHPSEVAATIAAVREGWPDKRLVMVyqphrfsrtRDLYE--DFVKVL----------ADVDQLLlldvys 405
Cdd:PRK11929 835 GTRIIDDTYNANPDSMRAAIDVLAELPNGPRALVL---------GDMLElgDNGPAMhrevgkyarqLGIDALI------ 899
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 746445361 406 agedpIVGADSKSLCRSLRQRGkePLHVATNAELAGVLAANLQNNDLVLTQG 457
Cdd:PRK11929 900 -----TLGEAARDAAAAFGAGA--RGVCASVDEIIAALRGALPEGDSVLIKG 944
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
323-414 |
2.47e-12 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 62.75 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 323 IGRRFQHYGEFenerGNVMLVDDYGHHPSEVAATIAAVREgWPDKRLVMVYQPHRfSRTRDLYEDFVKVLADV-DQLLLL 401
Cdd:pfam02875 1 VPGRLEVVGEN----NGVLVIDDYAHNPDAMEAALRALRN-LFPGRLILVFGGMG-DRDAEFHALLGRLAAALaDVVILT 74
|
90
....*....|...
gi 746445361 402 DVYSAGEDPIVGA 414
Cdd:pfam02875 75 GDYPRAEDPGAII 87
|
|
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
121-395 |
3.03e-11 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 65.13 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 121 IAIAGTHGKTTTTSLIASIYGQAGL-----------DPT--FIIGGllnsagsnAKVGKSDF---------LIAEADESD 178
Cdd:COG0285 43 IHVAGTNGKGSTAAMLESILRAAGYrvglytsphlvRFNerIRING--------EPISDEELvealeevepAVEEVDAGP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 179 AS---------FLH------------------------LQPMVSVITNIEEDHMDTYGGSLEK--------MKDtyvdfi 217
Cdd:COG0285 115 PTffevttaaaFLYfaeapvdvavlevglggrldatnvIDPLVSVITSIGLDHTDFLGDTLEEiarekagiIKP------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 218 hnlpfyGLAVVC--IDSEVAAELIPR---FGRPVITYGEskdaDYRMSDFSQSantcTFTVTNKQGECLTATLNMPGRHN 292
Cdd:COG0285 189 ------GVPVVTgdQQPEALEVIEERaaeLGAPLYRAGR----DFSVEEREGA----VFSYQGPGGEYEDLPLPLLGAHQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 293 ALNATAAIAVAK-----DQNIANHAILEALQKFEGIGRrfqhygeFENERGNVMLVDDYGHHPSEVAATIAAVREGWPDK 367
Cdd:COG0285 255 AENAALALAALEalrelGLPISEEAIREGLANARWPGR-------LEVLSRGPLVILDGAHNPAGARALAETLKELFPFR 327
|
330 340 350
....*....|....*....|....*....|
gi 746445361 368 RLVMVyqphrFS--RTRDlYEDFVKVLADV 395
Cdd:COG0285 328 KLHLV-----FGmlADKD-IEGMLAALAPL 351
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
184-358 |
3.87e-07 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 52.47 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 184 LQPMVSVITNIEEDHMDTYGGsLEKMKDTYVDFIHNLPFYGLAVVCIDSEVAAELIPRFGRP----VITYGESKDADYRM 259
Cdd:PRK14093 182 VRPHVAIITTVEPVHLEFFSG-IEAIADAKAEIFTGLEPGGAAVLNRDNPQFDRLAASARAAgiarIVSFGADEKADARL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 260 SDFSQSANtCTFTVTNKQGECLTATLNMPGRHNALNATAAIAVAK----DQNIANHAiLEALQKFEGIGRRFQhygeFEN 335
Cdd:PRK14093 261 LDVALHAD-CSAVHADILGHDVTYKLGMPGRHIAMNSLAVLAAAElagaDLALAALA-LSQVQPAAGRGVRHT----LEV 334
|
170 180
....*....|....*....|....
gi 746445361 336 ERGNVMLVDD-YGHHPSEVAATIA 358
Cdd:PRK14093 335 GGGEATLIDEsYNANPASMAAALG 358
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
184-373 |
4.05e-07 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 52.29 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 184 LQPMVSVITNIEEDHMDTYGGSLEK--------MKDTYVDFIHNLPFYGLAVVcidSEVAAELiprfGRPVITYGesKDA 255
Cdd:TIGR01499 130 IEPLVSVITSIGLDHTEILGDTLEEiawekagiIKEGVPIVTGEQEPEALNVL---KKKAQEK----GAPLFVVG--RDF 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 256 DYRMSDfsqsANTCTFTVTNKQGECLTATLnmPGRHNALNATAAIAVAKDQNIANHAILEALqKFEGIGrRFQHYGEFEN 335
Cdd:TIGR01499 201 NYSETD----ENYLSFSGANLFLEPLALSL--LGDHQQENAALALAALEVLGKQNPKLSEEA-IRQGLA-NTIWPGRLEI 272
|
170 180 190
....*....|....*....|....*....|....*....
gi 746445361 336 -ERGNVMLVDDYGHHPSEVAATIAAVREGWPDKRLVMVY 373
Cdd:TIGR01499 273 lSEDNPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLF 311
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
98-145 |
6.34e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.53 E-value: 6.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 746445361 98 KAARIPVVrraemlaelmrfrhgiAIAGTHGKTTTTSLIASIYGQAGL 145
Cdd:PRK14016 476 DDGRIPIV----------------AVTGTNGKTTTTRLIAHILKLSGK 507
|
|
| murF |
PRK10773 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed |
121-318 |
5.10e-04 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
Pssm-ID: 182718 [Multi-domain] Cd Length: 453 Bit Score: 42.33 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 121 IAIAGTHGKTTTTSLIASIYGQAGldptfiigGLLNSAGS-NAKVGKSDFLIAEADESDASFLHL--------------- 184
Cdd:PRK10773 103 VALTGSSGKTSVKEMTAAILRQCG--------NTLYTAGNlNNDIGVPLTLLRLTPEHDYAVIELganhqgeiaytvslt 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746445361 185 QPMVSVITNIEEDHMDTYGgSLEKMKDTYVDFIHNLPFYGLAVVCIDSE--------VAAELIPRFgrpviTYGESKDAD 256
Cdd:PRK10773 175 RPEAALVNNLAAAHLEGFG-SLAGVAKAKGEIFSGLPENGIAIMNADSNdwlnwqsvIGSKTVWRF-----SPNAANSVD 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 746445361 257 YRMSDFSQSANTCTFTVTNKQGEClTATLNMPGRHNALNATAAIAVAkdqnIANHAILEALQ 318
Cdd:PRK10773 249 FTATNIHVTSHGTEFTLHTPTGSV-DVLLPLPGRHNIANALAAAALA----MSVGATLDAVK 305
|
|
| |
